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161 related items for PubMed ID: 33965839

  • 1. Spectroscopic and biochemical characterization of metallo-β-lactamase IMP-1 with dicarboxylic, sulfonyl, and thiol inhibitors.
    Zhang H, Yang K, Cheng Z, Thomas C, Steinbrunner A, Pryor C, Vulcan M, Kemp C, Orea D, Paththamperuma C, Chen AY, Cohen SM, Page RC, Tierney DL, Crowder MW.
    Bioorg Med Chem; 2021 Jun 15; 40():116183. PubMed ID: 33965839
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  • 2. Probing the mechanisms of inhibition for various inhibitors of metallo-β-lactamases VIM-2 and NDM-1.
    Thomas CA, Cheng Z, Yang K, Hellwarth E, Yurkiewicz CJ, Baxter FM, Fullington SA, Klinsky SA, Otto JL, Chen AY, Cohen SM, Crowder MW.
    J Inorg Biochem; 2020 Sep 15; 210():111123. PubMed ID: 32622213
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  • 3. Design, synthesis, and in vitro and biological evaluation of potent amino acid-derived thiol inhibitors of the metallo-β-lactamase IMP-1.
    Arjomandi OK, Hussein WM, Vella P, Yusof Y, Sidjabat HE, Schenk G, McGeary RP.
    Eur J Med Chem; 2016 May 23; 114():318-27. PubMed ID: 27017264
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  • 4. Synthesis and enzyme-based evaluation of analogues L-tyrosine thiol carboxylic acid inhibitor of metallo-β-lactamase IMP-1.
    Khalili Arjomandi O, Kavoosi M, Adibi H.
    J Enzyme Inhib Med Chem; 2019 Dec 23; 34(1):1414-1425. PubMed ID: 31401901
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  • 8. Probing the Interaction of Aspergillomarasmine A with Metallo-β-lactamases NDM-1, VIM-2, and IMP-7.
    Bergstrom A, Katko A, Adkins Z, Hill J, Cheng Z, Burnett M, Yang H, Aitha M, Mehaffey MR, Brodbelt JS, Tehrani KHME, Martin NI, Bonomo RA, Page RC, Tierney DL, Fast W, Wright GD, Crowder MW.
    ACS Infect Dis; 2018 Feb 09; 4(2):135-145. PubMed ID: 29091730
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  • 9. Structural and kinetic studies on metallo-β-lactamase IMP-1.
    Griffin DH, Richmond TK, Sanchez C, Moller AJ, Breece RM, Tierney DL, Bennett B, Crowder MW.
    Biochemistry; 2011 Oct 25; 50(42):9125-34. PubMed ID: 21928807
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  • 13. Hydroxyhexylitaconic acids as potent IMP-type metallo-β-lactamase inhibitors for controlling carbapenem resistance in Enterobacterales.
    Wachino J-i, Jin W, Norizuki C, Kimura K, Tsuji M, Kurosaki H, Arakawa Y.
    Microbiol Spectr; 2024 Mar 05; 12(3):e0234423. PubMed ID: 38315122
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  • 15. In vitro potentiation of carbapenems with ME1071, a novel metallo-beta-lactamase inhibitor, against metallo-beta-lactamase- producing Pseudomonas aeruginosa clinical isolates.
    Ishii Y, Eto M, Mano Y, Tateda K, Yamaguchi K.
    Antimicrob Agents Chemother; 2010 Sep 05; 54(9):3625-9. PubMed ID: 20606062
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  • 16. Multiyear, Multinational Survey of the Incidence and Global Distribution of Metallo-β-Lactamase-Producing Enterobacteriaceae and Pseudomonas aeruginosa.
    Kazmierczak KM, Rabine S, Hackel M, McLaughlin RE, Biedenbach DJ, Bouchillon SK, Sahm DF, Bradford PA.
    Antimicrob Agents Chemother; 2016 Feb 05; 60(2):1067-78. PubMed ID: 26643349
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  • 17. Investigation of Dipicolinic Acid Isosteres for the Inhibition of Metallo-β-Lactamases.
    Chen AY, Thomas PW, Cheng Z, Xu NY, Tierney DL, Crowder MW, Fast W, Cohen SM.
    ChemMedChem; 2019 Jul 03; 14(13):1271-1282. PubMed ID: 31124602
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  • 18. Identification of bla(IMP-22) in Pseudomonas spp. in urban wastewater and nosocomial environments: biochemical characterization of a new IMP metallo-enzyme variant and its genetic location.
    Pellegrini C, Mercuri PS, Celenza G, Galleni M, Segatore B, Sacchetti E, Volpe R, Amicosante G, Perilli M.
    J Antimicrob Chemother; 2009 May 03; 63(5):901-8. PubMed ID: 19270313
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  • 19. Sulfamoyl Heteroarylcarboxylic Acids as Promising Metallo-β-Lactamase Inhibitors for Controlling Bacterial Carbapenem Resistance.
    Wachino JI, Jin W, Kimura K, Kurosaki H, Sato A, Arakawa Y.
    mBio; 2020 Mar 17; 11(2):. PubMed ID: 32184250
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  • 20. Inhibition of IMP-1 metallo-beta-lactamase and sensitization of IMP-1-producing bacteria by thioester derivatives.
    Hammond GG, Huber JL, Greenlee ML, Laub JB, Young K, Silver LL, Balkovec JM, Pryor KD, Wu JK, Leiting B, Pompliano DL, Toney JH.
    FEMS Microbiol Lett; 1999 Oct 15; 179(2):289-96. PubMed ID: 10518728
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